Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and 1 in Soybean.

@article{Matsusaki2016CooperativePF,
  title={Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and 1 in Soybean.},
  author={Motonori Matsusaki and Aya Okuda and Taro Masuda and Katsunori Koishihara and Ryuta Mita and Kensuke Iwasaki and Kumiko Hara and Yurika Naruo and Akiho Hirose and Yuichiro Tsuchi and Reiko Urade},
  journal={Plant physiology},
  year={2016},
  volume={170 2},
  pages={774-89}
}
Most proteins produced in the endoplasmic reticulum (ER) of eukaryotic cells fold via disulfide formation (oxidative folding). Oxidative folding is catalyzed by protein disulfide isomerase (PDI) and PDI-related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). In yeast and mammals, ER oxidoreductin-1s (Ero1s) supply oxidizing equivalent to the active centers of PDI. In this study, we expressed recombinant soybean Ero1 (GmERO1a) and found that GmERO1a oxidized multiple soybean ER… CONTINUE READING
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